Evidence map›Paper›PMID 26880549›Full record

ArticleeLife2016

Membrane palmitoylated protein 2 is a synaptic scaffold protein required for synaptic SK2-containing channel function.

Gukhan Kim, Rafael Luján, Jochen Schwenk, Melissa H Kelley, Carolina Aguado, Masahiko Watanabe, Bernd Fakler, James Maylie, John P Adelman

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.7field-weighted citation impact, top 33% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 25 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 4 countries.

Gukhan KimVollum Institute, Oregon Health and Science University, Portland, United States.
Rafael LujánInstituto de Investigación en Discapacidades Neurológicas, Departamento de Ciencias Médicas, Facultad de Medicina, Universidad de Castilla-La Mancha, Albacete, Spain.
Jochen SchwenkInstitute of Physiology, University of Freiburg, Freiburg, Germany.
Melissa H KelleyVollum Institute, Oregon Health and Science University, Portland, United States.
Carolina AguadoInstituto de Investigación en Discapacidades Neurológicas, Departamento de Ciencias Médicas, Facultad de Medicina, Universidad de Castilla-La Mancha, Albacete, Spain.
Masahiko WatanabeDepartment of Anatomy, Hokkaido University School of Medicine, Sapporo, Japan.
Bernd FaklerInstitute of Physiology, University of Freiburg, Freiburg, Germany.
James MaylieDepartment of Obstetrics and Gynecology, Oregon Health and Science University, Portland, United States.
John P AdelmanVollum Institute, Oregon Health and Science University, Portland, United States.ORCID http://orcid.org/0000-0002-1135-1549
Oregon Health & Science University · USUniversity of Castilla-La Mancha · ESUniversity of Freiburg · DEHokkaido University · JP

Funding

Molecular Physiology of the SK2 Channels in CA1 NeuronsR01NS038880 · NINDS · OREGON HEALTH & SCIENCE UNIVERSITY · PI MAYLIE, JAMES G · 2000 to 2017
$6.0M
Coupled LTP-dependent trafficking of synaptic SK channels and NMDARsR01MH093599 · NIMH · OREGON HEALTH & SCIENCE UNIVERSITY · PI ADELMAN, JOHN P, MAYLIE, JAMES G · 2012 to 2015
$1.2M
NIMH NIH HHS MH093599NIMH NIH HHS R01 MH093599NINDS NIH HHS NS038880NINDS NIH HHS R01 NS038880
6 · The paper itself

Abstract

Mouse CA1 pyramidal neurons express apamin-sensitive SK2-containing channels in the post-synaptic membrane, positioned close to NMDA-type (N-methyl-D-aspartate) glutamate receptors. Activated by synaptically evoked NMDAR-dependent Ca(2+) influx, the synaptic SK2-containing channels modulate excitatory post-synaptic responses and the induction of synaptic plasticity. In addition, their activity- and protein kinase A-dependent trafficking contributes to expression of long-term potentiation (LTP). We have identified a novel synaptic scaffold, MPP2 (membrane palmitoylated protein 2; p55), a member of the membrane-associated guanylate kinase (MAGUK) family that interacts with SK2-containing channels. MPP2 and SK2 co-immunopurified from mouse brain, and co-immunoprecipitated when they were co-expressed in HEK293 cells. MPP2 is highly expressed in the post-synaptic density of dendritic spines on CA1 pyramidal neurons. Knocking down MPP2 expression selectively abolished the SK2-containing channel contribution to synaptic responses and decreased LTP. Thus, MPP2 is a novel synaptic scaffold that is required for proper synaptic localization and function of SK2-containing channels.

Indexed as

AnimalsCA1 Region, HippocampalCell LineGuanylate KinasesHumansImmunoprecipitationMembrane ProteinsMiceProtein BindingPyramidal CellsSmall-Conductance Calcium-Activated Potassium ChannelsDlg2 protein, mouseGuanylate KinasesKcnn2 protein, mouseMembrane ProteinsSmall-Conductance Calcium-Activated Potassium Channelsmouseneurosciencesynaptic plasticitysynaptic scaffoldsynaptic transmission

Identifiers

PMID26880549
PMCPMC4764564
OpenAlexW2259340441

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.